› 1ymx

X-ray diffraction
1.7Å resolution

X-ray crystallographic structure of CTX-M-9 beta-lactamase covalently linked to cefoxitin

Released:
DOI: 10.2210/pdb1ymx/pdb
PDB entry 1ymx coloured by chain, front view.
PDB entry 1ymx coloured by chain, side view.
PDB entry 1ymx coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure, function, and inhibition along the reaction coordinate of CTX-M beta-lactamases.
Chen Y, Shoichet B, Bonnet R
J Am Chem Soc 127 5423-34 (2005)
PMID: 15826180

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192212 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 27.97 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9L5C8 (Residues: 29-291; Coverage: 100%)
Gene names: RCS51_P0174, bla CTX-M-9, blaCTX-M-9, blaCTX-M-9a, blaCTX-M-9b
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand 1QL 2 x 1QL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 45.209Å b: 106.781Å c: 47.779Å
α: 90° β: 101.62° γ: 90°
R-values:
R R work R free
0.158 0.158 0.197
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Three decades of beta-lactamase inhibitors.
Drawz et al. (2010)
12 more

6 mentions without citation

Comparative biochemical and computational study of the role of naturally occurring mutations at Ambler positions 104 and 170 in GES β-lactamases.
Kotsakis et al. (2010)
5 more